SSH1_MOUSE
ID SSH1_MOUSE Reviewed; 1042 AA.
AC Q76I79; Q3TDG3; Q69ZM4; Q811E5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein phosphatase Slingshot homolog 1 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:14531860};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044};
DE AltName: Full=SSH-like protein 1;
DE Short=SSH-1L;
DE Short=mSSH-1L;
GN Name=Ssh1 {ECO:0000312|MGI:MGI:2686240}; Synonyms=Kiaa1298, Ssh1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-393.
RX PubMed=14531860; DOI=10.1046/j.1365-2443.2003.00678.x;
RA Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y.,
RA Niwa R., Uemura T., Mizuno K.;
RT "Differential activities, subcellular distribution and tissue expression
RT patterns of three members of Slingshot family phosphatases that
RT dephosphorylate cofilin.";
RL Genes Cells 8:811-824(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 539-1042 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-1042 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH LIMK1.
RX PubMed=15660133; DOI=10.1038/sj.emboj.7600543;
RA Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B.,
RA Sampath R., Bamburg J.R., Bernard O.;
RT "Interplay between components of a novel LIM kinase-slingshot phosphatase
RT complex regulates cofilin.";
RL EMBO J. 24:473-486(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein phosphatase which regulates actin filament dynamics.
CC Dephosphorylates and activates the actin binding/depolymerizing factor
CC cofilin, which subsequently binds to actin filaments and stimulates
CC their disassembly. Inhibitory phosphorylation of cofilin is mediated by
CC LIMK1, which may also be dephosphorylated and inactivated by this
CC protein. {ECO:0000269|PubMed:14531860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:14531860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000305|PubMed:14531860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Interacts with the 14-3-3 proteins YWHAB, YWHAG, YWHAQ, and
CC YWHAZ. Interaction with 14-3-3 proteins inhibits phosphatase activity
CC and also blocks recruitment to lamellipodia and stimulation by actin
CC (By similarity). Interacts with actin and this stimulates phosphatase
CC activity. Interacts with LIMK1. {ECO:0000250,
CC ECO:0000269|PubMed:14531860, ECO:0000269|PubMed:15660133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14531860}. Cleavage furrow {ECO:0000250}. Midbody
CC {ECO:0000250}. Note=Localized to the cleavage furrow and the midbody
CC during cytokinesis (By similarity). Also colocalizes with F-actin in
CC the cytoplasm and the cell periphery, which may allow local control of
CC actin dynamics at sites of cell locomotion. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q76I79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76I79-2; Sequence=VSP_016320;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney and thymus. Also
CC expressed at lower levels in liver, skeletal muscle, small intestine
CC and spleen. {ECO:0000269|PubMed:14531860}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in the embryo at 14.5 dpc.
CC {ECO:0000269|PubMed:14531860}.
CC -!- PTM: Phosphorylated. Inhibitory phosphorylation by PAK4 promotes
CC binding to YWHAZ. Phosphorylation at Ser-970 is decreased by stimuli
CC which promote actin reorganization and lamellipodia formation. Can be
CC dephosphorylated and activated by PPP3CA/calcineurin A. Phosphorylation
CC decreases immediately prior to telophase (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Tyrosine phosphatase activity has not been demonstrated
CC for this protein to date.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32422.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB099287; BAC97810.1; -; mRNA.
DR EMBL; AK173144; BAD32422.1; ALT_INIT; mRNA.
DR EMBL; AK155557; BAE33323.1; -; mRNA.
DR EMBL; AK170212; BAE41639.1; -; mRNA.
DR EMBL; AK171556; BAE42524.1; -; mRNA.
DR EMBL; BC046529; AAH46529.1; -; mRNA.
DR CCDS; CCDS19556.1; -. [Q76I79-1]
DR CCDS; CCDS89972.1; -. [Q76I79-2]
DR RefSeq; NP_932777.2; NM_198109.4. [Q76I79-1]
DR AlphaFoldDB; Q76I79; -.
DR SMR; Q76I79; -.
DR BioGRID; 231148; 4.
DR IntAct; Q76I79; 1.
DR STRING; 10090.ENSMUSP00000124312; -.
DR iPTMnet; Q76I79; -.
DR PhosphoSitePlus; Q76I79; -.
DR EPD; Q76I79; -.
DR jPOST; Q76I79; -.
DR MaxQB; Q76I79; -.
DR PaxDb; Q76I79; -.
DR PRIDE; Q76I79; -.
DR ProteomicsDB; 258737; -. [Q76I79-1]
DR ProteomicsDB; 258738; -. [Q76I79-2]
DR Antibodypedia; 18311; 208 antibodies from 24 providers.
DR DNASU; 231637; -.
DR Ensembl; ENSMUST00000112298; ENSMUSP00000107917; ENSMUSG00000042121. [Q76I79-2]
DR Ensembl; ENSMUST00000159592; ENSMUSP00000124312; ENSMUSG00000042121. [Q76I79-1]
DR GeneID; 231637; -.
DR KEGG; mmu:231637; -.
DR UCSC; uc008yyx.1; mouse. [Q76I79-1]
DR UCSC; uc008yyz.1; mouse. [Q76I79-2]
DR CTD; 54434; -.
DR MGI; MGI:2686240; Ssh1.
DR VEuPathDB; HostDB:ENSMUSG00000042121; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000156133; -.
DR HOGENOM; CLU_006650_1_0_1; -.
DR InParanoid; Q76I79; -.
DR OMA; KPPYKSC; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q76I79; -.
DR TreeFam; TF319444; -.
DR BioGRID-ORCS; 231637; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ssh1; mouse.
DR PRO; PR:Q76I79; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q76I79; protein.
DR Bgee; ENSMUSG00000042121; Expressed in internal carotid artery and 216 other tissues.
DR ExpressionAtlas; Q76I79; baseline and differential.
DR Genevisible; Q76I79; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0000902; P:cell morphogenesis; ISO:MGI.
DR GO; GO:0071318; P:cellular response to ATP; ISO:MGI.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; ISO:MGI.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:1904719; P:positive regulation of AMPA glutamate receptor clustering; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISO:MGI.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; ISO:MGI.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR043587; Phosphatase_SSH-like.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR043588; SSH-N.
DR InterPro; IPR027233; SSH1.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45864; PTHR45864; 1.
DR PANTHER; PTHR45864:SF5; PTHR45864:SF5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Hydrolase; Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WYL5"
FT CHAIN 2..1042
FT /note="Protein phosphatase Slingshot homolog 1"
FT /id="PRO_0000094842"
FT DOMAIN 249..304
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DOMAIN 308..449
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..1042
FT /note="Interaction with YWHAG"
FT /evidence="ECO:0000250"
FT REGION 915..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYL5"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYL5"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYL5"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYL5"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYL5"
FT VAR_SEQ 158..179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_016320"
FT MUTAGEN 393
FT /note="C->S: Abrogates phosphatase activity."
FT /evidence="ECO:0000269|PubMed:14531860"
FT CONFLICT 526
FT /note="E -> D (in Ref. 4; AAH46529)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="V -> A (in Ref. 3; BAE41639)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="D -> E (in Ref. 3; BAE41639)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="A -> V (in Ref. 4; AAH46529)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="E -> G (in Ref. 3; BAE41639)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="S -> N (in Ref. 4; AAH46529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1042 AA; 115297 MW; 19A34E4937FA48FA CRC64;
MALVTLQRSP TPSAASSSAS NSELEAGSDE ERKLNLSLSE SFFMVKGAAL FLQQGNSPQG
QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESV WTDRVRYMVV VYTSGRQDTE
ENILLGVDFS SKESKSCTIG MVLRLWSDTK IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS
ALQVLHKACE VARRHNYFPG GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL
FVDKPTEGER TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE FKEFIDNEML
LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP GLFAYHNIRV
YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS ASTVIAYAMK EFGWPLEKAY
NYVKQKRSIT RPNAGFMRQL SEYEGILDAS KQRHNKLWRQ QPTDDTIAEP SEFLPETLDG
ALDAQLPCLD DTTHPGLPRS LAPGGPALPC CFRRLSDPLL LPHHDETGGL VHLEDLEKDA
LLEEEESQPV EVHKLVQHPQ EGARLCEKDV KRKLEFGNSK PRSDSLPQVE ELEKDGSPRT
GRWRRASTQL DRSLLDQENL NNNNSKRSCP DDLERDAMFG ILSKVKPPYT SCADCMYPTA
GGTPEAYMER HEDPSSSAIC TQPTFLPHVT SSPMAHASSR SRAPERPASG PANTSPFLLP
AGSRKPDVSG SGAGAAPEPP ASLLEPSRET SKALPKSLQL KNPHCDKNAA NMEVSAKEEP
SPKKDPKPAK DLRLLFSNEA EKPTTNSYLM QHQESIIQLQ KAGLVRKHTK ELERLKSLPS
DSPAACRDSA TCRLEASIPE EGSQEPAHPA LCSQAGSEEQ PVGGTLQKSP TSTLPRLDHT
SNFSKDFLKT VCYTPTSSSI SSNLTRSSSS DSIHSVRGKP GLVKQRAQEI ETRLRLAGLT
VSSPLKRSHS LAKLGSLNFS TEDLSSEADT STIADSQDAK CGLSSSFLPE PQSAPRDPAA
TSKSSGKSAP EHLKSPSRVN KS
